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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

Overview

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Updated: Jun 23, 2026

4D Imaging of Protein Aggregation in Live Cells
08:59

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

Tightly Knotted Enzymes Inhibit Protein-Protein Aggregation.

Susmita Sarkar, Hemanth Mandya Nagaiah, Michael L Klein

    Biorxiv : the Preprint Server for Biology
    |June 22, 2026
    PubMed
    Summary
    This summary is machine-generated.

    Protein backbone topology significantly impacts neurodegenerative disease risk. Intact protein knots suppress liquid-liquid phase separation (LLPS), while destabilized knots promote aggregation, linking topological stability to disease mechanisms.

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    Last Updated: Jun 23, 2026

    4D Imaging of Protein Aggregation in Live Cells
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    Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans

    Published on: December 17, 2021

    Area of Science:

    • Biophysics
    • Molecular Biology
    • Neuroscience

    Background:

    • Neurodegenerative diseases are linked to protein aggregation due to proteostasis failure.
    • The physical factors driving transitions from soluble states to liquid-liquid phase separation (LLPS) and aggregation are not fully understood.

    Purpose of the Study:

    • To investigate the influence of protein backbone topology on phase behavior.
    • To explore the role of ubiquitin C-terminal hydrolase L1 (UCH-L1) and its Parkinson's disease-associated mutant (I93M) in phase transitions.

    Main Methods:

    • Multiscale molecular dynamics (MD) simulations of single-chain and multichain systems.
    • Analysis of conformational ensembles, intermolecular contacts, and dynamic properties.

    Main Results:

    • Knot integrity in UCH-L1 constrains conformation, limiting expanded states and suppressing LLPS.
    • Destabilization of the UCH-L1 knot in the I93M mutant enhances intermolecular contacts and stabilizes protein-rich phases.
    • Intact topology leads to liquid-like condensates, while destabilized topology results in viscoelastic assemblies with slower dynamics.

    Conclusions:

    • Protein topological integrity is a critical determinant of protein phase behavior.
    • A mechanistic link exists between topological stability and the material properties of protein condensates.
    • These findings have implications for understanding aggregation-associated neurodegenerative diseases.